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1tet

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Revision as of 09:26, 29 September 2021

CRYSTAL STRUCTURE OF AN ANTICHOLERA TOXIN PEPTIDE COMPLEX AT 2.3 ANGSTROMS

Structural highlights

1tet is a 3 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ELBP_ECOLX] The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Cholera toxin peptide 3 (CTP3) is a 15-residue peptide corresponding in sequence to an immunogenic loop on the surface of the B-subunits of both cholera toxin and the heat-labile toxin from Escherichia coli. TE33 is the Fab fragment of a monoclonal antibody elicited against CTP3. The crystal structure of the TE33-CTP3 complex at 2.3 A resolution reveals an antigen-binding pocket, 13 A deep and 13 A wide, which is lined with many aromatic residues. The N-terminal portion of the peptide antigen CTP3 forms a type II beta-turn that fits snugly into this pocket. At gln7 the peptide backbone of CTP3 forms a kink followed by an extended C-terminal chain that seals off the cleft and buries the beta-turn underneath it. All six complementarity-determining regions of TE33 contribute to the binding of CTP3. The antibody-peptide contacts include, in addition to van der Waals' interactions and hydrogen bonds, also one salt bridge and one water molecule, which mediates the interaction.

Crystal structure of an anticholera toxin peptide complex at 2.3 A.,Shoham M J Mol Biol. 1993 Aug 20;232(4):1169-75. PMID:7690406^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Shoham M. Crystal structure of an anticholera toxin peptide complex at 2.3 A. J Mol Biol. 1993 Aug 20;232(4):1169-75. PMID:7690406 doi:http://dx.doi.org/10.1006/jmbi.1993.1469

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1tet"

Categories: Large Structures | Mus musculus | Shoham, M | Immunoglobulin

@@ Line 3: / Line 3: @@
 <StructureSection load='1tet' size='340' side='right'caption='[[1tet]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1tet]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TET OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TET FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1tet]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TET OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TET FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tet OCA], [http://pdbe.org/1tet PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tet RCSB], [http://www.ebi.ac.uk/pdbsum/1tet PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tet ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tet OCA], [https://pdbe.org/1tet PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tet RCSB], [https://www.ebi.ac.uk/pdbsum/1tet PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tet ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ELBP_ECOLX ELBP_ECOLX]] The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase.
+[[https://www.uniprot.org/uniprot/ELBP_ECOLX ELBP_ECOLX]] The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 *[[Antibody 3D structures|Antibody 3D structures]]
 *[[User:David Solfiell/sandbox 1|User:David Solfiell/sandbox 1]]
+*[[3D structures of non-human antibody|3D structures of non-human antibody]]
 == References ==
 <references/>

1tet

From Proteopedia

Revision as of 09:26, 29 September 2021

CRYSTAL STRUCTURE OF AN ANTICHOLERA TOXIN PEPTIDE COMPLEX AT 2.3 ANGSTROMS

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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